Literature references that cite this PDB file's
key reference
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PubMed id
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Reference
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H.Wu,
J.Min,
V.V.Lunin,
T.Antoshenko,
L.Dombrovski,
H.Zeng,
A.Allali-Hassani,
V.Campagna-Slater,
M.Vedadi,
C.H.Arrowsmith,
A.N.Plotnikov,
and
M.Schapira
(2010).
Structural biology of human H3K9 methyltransferases.
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PLoS One, 5,
e8570.
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PDB codes:
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C.K.Ea,
and
D.Baltimore
(2009).
Regulation of NF-kappaB activity through lysine monomethylation of p65.
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Proc Natl Acad Sci U S A, 106,
18972-18977.
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L.Colin,
and
C.Van Lint
(2009).
Molecular control of HIV-1 postintegration latency: implications for the development of new therapeutic strategies.
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Retrovirology, 6,
111.
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Q.Xu,
Y.Z.Chu,
H.B.Guo,
J.C.Smith,
and
H.Guo
(2009).
Energy triplets for writing epigenetic marks: insights from QM/MM free-energy simulations of protein lysine methyltransferases.
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Chemistry, 15,
12596-12599.
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R.A.Copeland,
M.E.Solomon,
and
V.M.Richon
(2009).
Protein methyltransferases as a target class for drug discovery.
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Nat Rev Drug Discov, 8,
724-732.
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S.Raunser,
R.Magnani,
Z.Huang,
R.L.Houtz,
R.C.Trievel,
P.A.Penczek,
and
T.Walz
(2009).
Rubisco in complex with Rubisco large subunit methyltransferase.
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Proc Natl Acad Sci U S A, 106,
3160-3165.
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Y.Chang,
X.Zhang,
J.R.Horton,
A.K.Upadhyay,
A.Spannhoff,
J.Liu,
J.P.Snyder,
M.T.Bedford,
and
X.Cheng
(2009).
Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294.
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Nat Struct Mol Biol, 16,
312-317.
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PDB code:
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Y.H.Takahashi,
J.S.Lee,
S.K.Swanson,
A.Saraf,
L.Florens,
M.P.Washburn,
R.C.Trievel,
and
A.Shilatifard
(2009).
Regulation of H3K4 trimethylation via Cps40 (Spp1) of COMPASS is monoubiquitination independent: implication for a Phe/Tyr switch by the catalytic domain of Set1.
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Mol Cell Biol, 29,
3478-3486.
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A.Patel,
V.E.Vought,
V.Dharmarajan,
and
M.S.Cosgrove
(2008).
A Conserved Arginine-containing Motif Crucial for the Assembly and Enzymatic Activity of the Mixed Lineage Leukemia Protein-1 Core Complex.
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J Biol Chem, 283,
32162-32175.
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B.D.Beck,
S.J.Park,
Y.J.Lee,
Y.Roman,
R.A.Hromas,
and
S.H.Lee
(2008).
Human Pso4 is a metnase (SETMAR)-binding partner that regulates metnase function in DNA repair.
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J Biol Chem, 283,
9023-9030.
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C.S.Veerappan,
Z.Avramova,
and
E.N.Moriyama
(2008).
Evolution of SET-domain protein families in the unicellular and multicellular Ascomycota fungi.
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BMC Evol Biol, 8,
190.
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F.Frederiks,
M.Tzouros,
G.Oudgenoeg,
T.van Welsem,
M.Fornerod,
J.Krijgsveld,
and
F.van Leeuwen
(2008).
Nonprocessive methylation by Dot1 leads to functional redundancy of histone H3K79 methylation states.
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Nat Struct Mol Biol, 15,
550-557.
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G.Brosch,
P.Loidl,
and
S.Graessle
(2008).
Histone modifications and chromatin dynamics: a focus on filamentous fungi.
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FEMS Microbiol Rev, 32,
409-439.
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J.F.Couture,
L.M.Dirk,
J.S.Brunzelle,
R.L.Houtz,
and
R.C.Trievel
(2008).
Structural origins for the product specificity of SET domain protein methyltransferases.
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Proc Natl Acad Sci U S A, 105,
20659-20664.
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PDB codes:
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K.K.Adhvaryu,
and
E.U.Selker
(2008).
Protein phosphatase PP1 is required for normal DNA methylation in Neurospora.
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Genes Dev, 22,
3391-3396.
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L.Xu,
Z.Zhao,
A.Dong,
L.Soubigou-Taconnat,
J.P.Renou,
A.Steinmetz,
and
W.H.Shen
(2008).
Di- and tri- but not monomethylation on histone H3 lysine 36 marks active transcription of genes involved in flowering time regulation and other processes in Arabidopsis thaliana.
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Mol Cell Biol, 28,
1348-1360.
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P.Joshi,
E.A.Carrington,
L.Wang,
C.S.Ketel,
E.L.Miller,
R.S.Jones,
and
J.A.Simon
(2008).
Dominant Alleles Identify SET Domain Residues Required for Histone Methyltransferase of Polycomb Repressive Complex 2.
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J Biol Chem, 283,
27757-27766.
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V.Krauss
(2008).
Glimpses of evolution: heterochromatic histone H3K9 methyltransferases left its marks behind.
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Genetica, 133,
93.
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X.Zhang,
and
T.C.Bruice
(2008).
Enzymatic mechanism and product specificity of SET-domain protein lysine methyltransferases.
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Proc Natl Acad Sci U S A, 105,
5728-5732.
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Y.Li,
M.A.Reddy,
F.Miao,
N.Shanmugam,
J.K.Yee,
D.Hawkins,
B.Ren,
and
R.Natarajan
(2008).
Role of the histone H3 lysine 4 methyltransferase, SET7/9, in the regulation of NF-kappaB-dependent inflammatory genes. Relevance to diabetes and inflammation.
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J Biol Chem, 283,
26771-26781.
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C.F.Sautel,
D.Cannella,
O.Bastien,
S.Kieffer,
D.Aldebert,
J.Garin,
I.Tardieux,
H.Belrhali,
and
M.A.Hakimi
(2007).
SET8-mediated methylations of histone H4 lysine 20 mark silent heterochromatic domains in apicomplexan genomes.
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Mol Cell Biol, 27,
5711-5724.
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H.B.Guo,
and
H.Guo
(2007).
Mechanism of histone methylation catalyzed by protein lysine methyltransferase SET7/9 and origin of product specificity.
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Proc Natl Acad Sci U S A, 104,
8797-8802.
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H.Demirci,
S.T.Gregory,
A.E.Dahlberg,
and
G.Jogl
(2007).
Recognition of ribosomal protein L11 by the protein trimethyltransferase PrmA.
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EMBO J, 26,
567-577.
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PDB codes:
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J.A.Casas-Mollano,
K.van Dijk,
J.Eisenhart,
and
H.Cerutti
(2007).
SET3p monomethylates histone H3 on lysine 9 and is required for the silencing of tandemly repeated transgenes in Chlamydomonas.
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Nucleic Acids Res, 35,
939-950.
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K.L.Rice,
I.Hormaeche,
and
J.D.Licht
(2007).
Epigenetic regulation of normal and malignant hematopoiesis.
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Oncogene, 26,
6697-6714.
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M.Yang,
J.C.Culhane,
L.M.Szewczuk,
C.B.Gocke,
C.A.Brautigam,
D.R.Tomchick,
M.Machius,
P.A.Cole,
and
H.Yu
(2007).
Structural basis of histone demethylation by LSD1 revealed by suicide inactivation.
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Nat Struct Mol Biol, 14,
535-539.
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PDB code:
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S.Lall
(2007).
Primers on chromatin.
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Nat Struct Mol Biol, 14,
1110-1115.
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Z.Chen,
J.Zang,
J.Kappler,
X.Hong,
F.Crawford,
Q.Wang,
F.Lan,
C.Jiang,
J.Whetstine,
S.Dai,
K.Hansen,
Y.Shi,
and
G.Zhang
(2007).
Structural basis of the recognition of a methylated histone tail by JMJD2A.
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Proc Natl Acad Sci U S A, 104,
10818-10823.
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PDB codes:
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A.J.Ruthenburg,
W.Wang,
D.M.Graybosch,
H.Li,
C.D.Allis,
D.J.Patel,
and
G.L.Verdine
(2006).
Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex.
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Nat Struct Mol Biol, 13,
704-712.
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PDB codes:
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B.D.Fodor,
S.Kubicek,
M.Yonezawa,
R.J.O'Sullivan,
R.Sengupta,
L.Perez-Burgos,
S.Opravil,
K.Mechtler,
G.Schotta,
and
T.Jenuwein
(2006).
Jmjd2b antagonizes H3K9 trimethylation at pericentric heterochromatin in mammalian cells.
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Genes Dev, 20,
1557-1562.
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J.F.Couture,
E.Collazo,
G.Hauk,
and
R.C.Trievel
(2006).
Structural basis for the methylation site specificity of SET7/9.
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Nat Struct Mol Biol, 13,
140-146.
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PDB code:
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J.F.Couture,
G.Hauk,
M.J.Thompson,
G.M.Blackburn,
and
R.C.Trievel
(2006).
Catalytic roles for carbon-oxygen hydrogen bonding in SET domain lysine methyltransferases.
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J Biol Chem, 281,
19280-19287.
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PDB codes:
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J.Mis,
S.S.Ner,
and
T.A.Grigliatti
(2006).
Identification of three histone methyltransferases in Drosophila: dG9a is a suppressor of PEV and is required for gene silencing.
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Mol Genet Genomics, 275,
513-526.
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M.Stabell,
M.Bjørkmo,
R.B.Aalen,
and
A.Lambertsson
(2006).
The Drosophila SET domain encoding gene dEset is essential for proper development.
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Hereditas, 143,
177-188.
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M.Stabell,
R.Eskeland,
M.Bjørkmo,
J.Larsson,
R.B.Aalen,
A.Imhof,
and
A.Lambertsson
(2006).
The Drosophila G9a gene encodes a multi-catalytic histone methyltransferase required for normal development.
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Nucleic Acids Res, 34,
4609-4621.
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T.Jenuwein
(2006).
The epigenetic magic of histone lysine methylation.
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FEBS J, 273,
3121-3135.
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T.Thorstensen,
A.Fischer,
S.V.Sandvik,
S.S.Johnsen,
P.E.Grini,
G.Reuter,
and
R.B.Aalen
(2006).
The Arabidopsis SUVR4 protein is a nucleolar histone methyltransferase with preference for monomethylated H3K9.
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Nucleic Acids Res, 34,
5461-5470.
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V.Krauss,
A.Fassl,
P.Fiebig,
I.Patties,
and
H.Sass
(2006).
The evolution of the histone methyltransferase gene Su(var)3-9 in metazoans includes a fusion with and a re-fission from a functionally unrelated gene.
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BMC Evol Biol, 6,
18.
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Y.Tsukada,
J.Fang,
H.Erdjument-Bromage,
M.E.Warren,
C.H.Borchers,
P.Tempst,
and
Y.Zhang
(2006).
Histone demethylation by a family of JmjC domain-containing proteins.
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Nature, 439,
811-816.
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B.Xiao,
C.Jing,
G.Kelly,
P.A.Walker,
F.W.Muskett,
T.A.Frenkiel,
S.R.Martin,
K.Sarma,
D.Reinberg,
S.J.Gamblin,
and
J.R.Wilson
(2005).
Specificity and mechanism of the histone methyltransferase Pr-Set7.
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Genes Dev, 19,
1444-1454.
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PDB code:
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D.C.Drummond,
C.O.Noble,
D.B.Kirpotin,
Z.Guo,
G.K.Scott,
and
C.C.Benz
(2005).
Clinical development of histone deacetylase inhibitors as anticancer agents.
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Annu Rev Pharmacol Toxicol, 45,
495-528.
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I.M.Fingerman,
C.L.Wu,
B.D.Wilson,
and
S.D.Briggs
(2005).
Global loss of Set1-mediated H3 Lys4 trimethylation is associated with silencing defects in Saccharomyces cerevisiae.
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J Biol Chem, 280,
28761-28765.
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J.F.Couture,
E.Collazo,
J.S.Brunzelle,
and
R.C.Trievel
(2005).
Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase.
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Genes Dev, 19,
1455-1465.
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PDB code:
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K.K.Adhvaryu,
S.A.Morris,
B.D.Strahl,
and
E.U.Selker
(2005).
Methylation of histone H3 lysine 36 is required for normal development in Neurospora crassa.
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Eukaryot Cell, 4,
1455-1464.
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P.O.Estève,
D.Patnaik,
H.G.Chin,
J.Benner,
M.A.Teitell,
and
S.Pradhan
(2005).
Functional analysis of the N- and C-terminus of mammalian G9a histone H3 methyltransferase.
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Nucleic Acids Res, 33,
3211-3223.
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R.E.Collins,
M.Tachibana,
H.Tamaru,
K.M.Smith,
D.Jia,
X.Zhang,
E.U.Selker,
Y.Shinkai,
and
X.Cheng
(2005).
In vitro and in vivo analyses of a Phe/Tyr switch controlling product specificity of histone lysine methyltransferases.
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J Biol Chem, 280,
5563-5570.
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R.Wu,
A.V.Terry,
P.B.Singh,
and
D.M.Gilbert
(2005).
Differential subnuclear localization and replication timing of histone H3 lysine 9 methylation states.
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Mol Biol Cell, 16,
2872-2881.
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S.C.Dillon,
X.Zhang,
R.C.Trievel,
and
X.Cheng
(2005).
The SET-domain protein superfamily: protein lysine methyltransferases.
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Genome Biol, 6,
227.
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S.H.Lee,
M.Oshige,
S.T.Durant,
K.K.Rasila,
E.A.Williamson,
H.Ramsey,
L.Kwan,
J.A.Nickoloff,
and
R.Hromas
(2005).
The SET domain protein Metnase mediates foreign DNA integration and links integration to nonhomologous end-joining repair.
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Proc Natl Acad Sci U S A, 102,
18075-18080.
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X.Cheng,
R.E.Collins,
and
X.Zhang
(2005).
Structural and sequence motifs of protein (histone) methylation enzymes.
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Annu Rev Biophys Biomol Struct, 34,
267-294.
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Y.Yin,
C.Liu,
S.N.Tsai,
B.Zhou,
S.M.Ngai,
and
G.Zhu
(2005).
SET8 recognizes the sequence RHRK20VLRDN within the N terminus of histone H4 and mono-methylates lysine 20.
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J Biol Chem, 280,
30025-30031.
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A.E.Ehrenhofer-Murray
(2004).
Chromatin dynamics at DNA replication, transcription and repair.
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| |
Eur J Biochem, 271,
2335-2349.
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D.J.Ebbole,
Y.Jin,
M.Thon,
H.Pan,
E.Bhattarai,
T.Thomas,
and
R.Dean
(2004).
Gene discovery and gene expression in the rice blast fungus, Magnaporthe grisea: analysis of expressed sequence tags.
|
| |
Mol Plant Microbe Interact, 17,
1337-1347.
|
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D.Patnaik,
H.G.Chin,
P.O.Estève,
J.Benner,
S.E.Jacobsen,
and
S.Pradhan
(2004).
Substrate specificity and kinetic mechanism of mammalian G9a histone H3 methyltransferase.
|
| |
J Biol Chem, 279,
53248-53258.
|
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K.Sawada,
Z.Yang,
J.R.Horton,
R.E.Collins,
X.Zhang,
and
X.Cheng
(2004).
Structure of the conserved core of the yeast Dot1p, a nucleosomal histone H3 lysine 79 methyltransferase.
|
| |
J Biol Chem, 279,
43296-43306.
|
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PDB code:
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L.M.Iyer,
and
L.Aravind
(2004).
The emergence of catalytic and structural diversity within the beta-clip fold.
|
| |
Proteins, 55,
977-991.
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M.J.Bottomley
(2004).
Structures of protein domains that create or recognize histone modifications.
|
| |
EMBO Rep, 5,
464-469.
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M.Lachner,
R.Sengupta,
G.Schotta,
and
T.Jenuwein
(2004).
Trilogies of histone lysine methylation as epigenetic landmarks of the eukaryotic genome.
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| |
Cold Spring Harb Symp Quant Biol, 69,
209-218.
|
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Z.Zhao,
and
W.H.Shen
(2004).
Plants contain a high number of proteins showing sequence similarity to the animal SUV39H family of histone methyltransferases.
|
| |
Ann N Y Acad Sci, 1030,
661-669.
|
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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